Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu
- Autores
- Barrantes, Francisco José
- Año de publicación
- 2022
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Fil: Barrantes, Francisco José. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; Argentina
Fil: Barrantes, Francisco José. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Abstract: Hampered by the diffraction phenomenon, as expressed in 1873 by Abbe, applications of optical microscopy to image biological structures were for a long time limited to resolutions above the ~200 nm barrier and restricted to the observation of stained specimens. The introduction of fluorescence was a game changer, and since its inception it became the gold standard technique in biological microscopy. The plasma membrane is a tenuous envelope of 4 nm–10 nm in thickness surrounding the cell. Because of its highly versatile spectroscopic properties and availability of suitable instrumentation, fluorescence techniques epitomize the current approach to study this delicate structure and its molecular constituents. The wide spectral range covered by fluorescence, intimately linked to the availability of appropriate intrinsic and extrinsic probes, provides the ability to dissect membrane constituents at the molecular scale in the spatial domain. In addition, the time resolution capabilities of fluorescence methods provide complementary high precision for studying the behavior of membrane molecules in the time domain. This review illustrates the value of various fluorescence techniques to extract information on the topography and motion of plasma membrane receptors. To this end I resort to a paradigmatic membrane-bound neurotransmitter receptor, the nicotinic acetylcholine receptor (nAChR). The structural and dynamic picture emerging from studies of this prototypic pentameric ligand-gated ion channel can be extrapolated not only to other members of this superfamily of ion channels but to other membrane-bound proteins. I also briefly discuss the various emerging techniques in the field of biomembrane labeling with new organic chemistry strategies oriented to applications in fluorescence nanoscopy, the form of fluorescence microscopy that is expanding the depth and scope of interrogation of membrane-associated phenomena. - Fuente
- Frontiers in Molecular Biosciences. 2022, 9:1014659
- Materia
-
MEMBRANA PLASMATICA
INTERACCIONES PROTEÍNA-PROTEÍNA
COLESTEROL
NANOSCOPIA
MICROSCOPIO FLUORESCENTE
RECEPTOR DE ACETILCOLINA - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/4.0/
- Repositorio
- Institución
- Pontificia Universidad Católica Argentina
- OAI Identificador
- oai:ucacris:123456789/18149
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Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieuBarrantes, Francisco JoséMEMBRANA PLASMATICAINTERACCIONES PROTEÍNA-PROTEÍNACOLESTEROLNANOSCOPIAMICROSCOPIO FLUORESCENTERECEPTOR DE ACETILCOLINAFil: Barrantes, Francisco José. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; ArgentinaFil: Barrantes, Francisco José. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaAbstract: Hampered by the diffraction phenomenon, as expressed in 1873 by Abbe, applications of optical microscopy to image biological structures were for a long time limited to resolutions above the ~200 nm barrier and restricted to the observation of stained specimens. The introduction of fluorescence was a game changer, and since its inception it became the gold standard technique in biological microscopy. The plasma membrane is a tenuous envelope of 4 nm–10 nm in thickness surrounding the cell. Because of its highly versatile spectroscopic properties and availability of suitable instrumentation, fluorescence techniques epitomize the current approach to study this delicate structure and its molecular constituents. The wide spectral range covered by fluorescence, intimately linked to the availability of appropriate intrinsic and extrinsic probes, provides the ability to dissect membrane constituents at the molecular scale in the spatial domain. In addition, the time resolution capabilities of fluorescence methods provide complementary high precision for studying the behavior of membrane molecules in the time domain. This review illustrates the value of various fluorescence techniques to extract information on the topography and motion of plasma membrane receptors. To this end I resort to a paradigmatic membrane-bound neurotransmitter receptor, the nicotinic acetylcholine receptor (nAChR). The structural and dynamic picture emerging from studies of this prototypic pentameric ligand-gated ion channel can be extrapolated not only to other members of this superfamily of ion channels but to other membrane-bound proteins. I also briefly discuss the various emerging techniques in the field of biomembrane labeling with new organic chemistry strategies oriented to applications in fluorescence nanoscopy, the form of fluorescence microscopy that is expanding the depth and scope of interrogation of membrane-associated phenomena.Frontiers Media2022info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://repositorio.uca.edu.ar/handle/123456789/1814910.3389/fmolb.2022.1014659Barrantes, F. J. Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu [en línea]. Frontiers in Molecular Biosciences. 2022, 9:1014659. doi: 10.3389/fmolb.2022.1014659. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/18149Frontiers in Molecular Biosciences. 2022, 9:1014659reponame:Repositorio Institucional (UCA)instname:Pontificia Universidad Católica Argentinaenginfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/4.0/2025-07-03T10:59:48Zoai:ucacris:123456789/18149instacron:UCAInstitucionalhttps://repositorio.uca.edu.ar/Universidad privadaNo correspondehttps://repositorio.uca.edu.ar/oaiclaudia_fernandez@uca.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:25852025-07-03 10:59:48.218Repositorio Institucional (UCA) - Pontificia Universidad Católica Argentinafalse |
dc.title.none.fl_str_mv |
Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu |
title |
Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu |
spellingShingle |
Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu Barrantes, Francisco José MEMBRANA PLASMATICA INTERACCIONES PROTEÍNA-PROTEÍNA COLESTEROL NANOSCOPIA MICROSCOPIO FLUORESCENTE RECEPTOR DE ACETILCOLINA |
title_short |
Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu |
title_full |
Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu |
title_fullStr |
Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu |
title_full_unstemmed |
Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu |
title_sort |
Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu |
dc.creator.none.fl_str_mv |
Barrantes, Francisco José |
author |
Barrantes, Francisco José |
author_facet |
Barrantes, Francisco José |
author_role |
author |
dc.subject.none.fl_str_mv |
MEMBRANA PLASMATICA INTERACCIONES PROTEÍNA-PROTEÍNA COLESTEROL NANOSCOPIA MICROSCOPIO FLUORESCENTE RECEPTOR DE ACETILCOLINA |
topic |
MEMBRANA PLASMATICA INTERACCIONES PROTEÍNA-PROTEÍNA COLESTEROL NANOSCOPIA MICROSCOPIO FLUORESCENTE RECEPTOR DE ACETILCOLINA |
dc.description.none.fl_txt_mv |
Fil: Barrantes, Francisco José. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; Argentina Fil: Barrantes, Francisco José. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Abstract: Hampered by the diffraction phenomenon, as expressed in 1873 by Abbe, applications of optical microscopy to image biological structures were for a long time limited to resolutions above the ~200 nm barrier and restricted to the observation of stained specimens. The introduction of fluorescence was a game changer, and since its inception it became the gold standard technique in biological microscopy. The plasma membrane is a tenuous envelope of 4 nm–10 nm in thickness surrounding the cell. Because of its highly versatile spectroscopic properties and availability of suitable instrumentation, fluorescence techniques epitomize the current approach to study this delicate structure and its molecular constituents. The wide spectral range covered by fluorescence, intimately linked to the availability of appropriate intrinsic and extrinsic probes, provides the ability to dissect membrane constituents at the molecular scale in the spatial domain. In addition, the time resolution capabilities of fluorescence methods provide complementary high precision for studying the behavior of membrane molecules in the time domain. This review illustrates the value of various fluorescence techniques to extract information on the topography and motion of plasma membrane receptors. To this end I resort to a paradigmatic membrane-bound neurotransmitter receptor, the nicotinic acetylcholine receptor (nAChR). The structural and dynamic picture emerging from studies of this prototypic pentameric ligand-gated ion channel can be extrapolated not only to other members of this superfamily of ion channels but to other membrane-bound proteins. I also briefly discuss the various emerging techniques in the field of biomembrane labeling with new organic chemistry strategies oriented to applications in fluorescence nanoscopy, the form of fluorescence microscopy that is expanding the depth and scope of interrogation of membrane-associated phenomena. |
description |
Fil: Barrantes, Francisco José. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; Argentina |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
https://repositorio.uca.edu.ar/handle/123456789/18149 10.3389/fmolb.2022.1014659 Barrantes, F. J. Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu [en línea]. Frontiers in Molecular Biosciences. 2022, 9:1014659. doi: 10.3389/fmolb.2022.1014659. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/18149 |
url |
https://repositorio.uca.edu.ar/handle/123456789/18149 |
identifier_str_mv |
10.3389/fmolb.2022.1014659 Barrantes, F. J. Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu [en línea]. Frontiers in Molecular Biosciences. 2022, 9:1014659. doi: 10.3389/fmolb.2022.1014659. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/18149 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/4.0/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/4.0/ |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Frontiers Media |
publisher.none.fl_str_mv |
Frontiers Media |
dc.source.none.fl_str_mv |
Frontiers in Molecular Biosciences. 2022, 9:1014659 reponame:Repositorio Institucional (UCA) instname:Pontificia Universidad Católica Argentina |
reponame_str |
Repositorio Institucional (UCA) |
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Repositorio Institucional (UCA) |
instname_str |
Pontificia Universidad Católica Argentina |
repository.name.fl_str_mv |
Repositorio Institucional (UCA) - Pontificia Universidad Católica Argentina |
repository.mail.fl_str_mv |
claudia_fernandez@uca.edu.ar |
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